1mgp

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(New page: 200px<br /><applet load="1mgp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mgp, resolution 2.00&Aring;" /> '''Hypothetical protein...)
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[[Image:1mgp.gif|left|200px]]<br /><applet load="1mgp" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1mgp.gif|left|200px]]<br /><applet load="1mgp" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mgp, resolution 2.00&Aring;" />
caption="1mgp, resolution 2.00&Aring;" />
'''Hypothetical protein TM841 from Thermotoga maritima reveals fatty acid binding function'''<br />
'''Hypothetical protein TM841 from Thermotoga maritima reveals fatty acid binding function'''<br />
==Overview==
==Overview==
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We determined the three-dimensional (3D) crystal structure of protein, TM841, a protein product from a hypothetical open-reading frame in the, genome of the hyperthermophile bacterium Thermotoga maritima, to 2.0 A, resolution. The protein belongs to a large protein family, DegV or COG1307, of unknown function. The 35 kDa protein consists of two separate domains, with low-level structural resemblance to domains from other proteins with, known 3D structures. These structural homologies, however, provided no, clues for the function of TM841. But the electron density maps revealed, clear density for a bound fatty-acid molecule in a pocket between the two, protein domains. The structure indicates that TM841 has the molecular, function of fatty-acid binding and may play a role in the cellular, functions of fatty acid transport or metabolism.
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We determined the three-dimensional (3D) crystal structure of protein TM841, a protein product from a hypothetical open-reading frame in the genome of the hyperthermophile bacterium Thermotoga maritima, to 2.0 A resolution. The protein belongs to a large protein family, DegV or COG1307 of unknown function. The 35 kDa protein consists of two separate domains, with low-level structural resemblance to domains from other proteins with known 3D structures. These structural homologies, however, provided no clues for the function of TM841. But the electron density maps revealed clear density for a bound fatty-acid molecule in a pocket between the two protein domains. The structure indicates that TM841 has the molecular function of fatty-acid binding and may play a role in the cellular functions of fatty acid transport or metabolism.
==About this Structure==
==About this Structure==
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1MGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with PLM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MGP OCA].
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1MGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=PLM:'>PLM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MGP OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: BSGC, Berkeley.Structural.Genomics.Center.]]
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[[Category: BSGC, Berkeley Structural Genomics Center.]]
[[Category: Kim, R.]]
[[Category: Kim, R.]]
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[[Category: Kim, S.H.]]
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[[Category: Kim, S H.]]
[[Category: Pelaschier, J.]]
[[Category: Pelaschier, J.]]
[[Category: Schulze-Gahmen, U.]]
[[Category: Schulze-Gahmen, U.]]
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[[Category: two domain structure with mixed alpha/beta structures in both domains]]
[[Category: two domain structure with mixed alpha/beta structures in both domains]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:24:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:59 2008''

Revision as of 11:55, 21 February 2008


1mgp, resolution 2.00Å

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Hypothetical protein TM841 from Thermotoga maritima reveals fatty acid binding function

Overview

We determined the three-dimensional (3D) crystal structure of protein TM841, a protein product from a hypothetical open-reading frame in the genome of the hyperthermophile bacterium Thermotoga maritima, to 2.0 A resolution. The protein belongs to a large protein family, DegV or COG1307 of unknown function. The 35 kDa protein consists of two separate domains, with low-level structural resemblance to domains from other proteins with known 3D structures. These structural homologies, however, provided no clues for the function of TM841. But the electron density maps revealed clear density for a bound fatty-acid molecule in a pocket between the two protein domains. The structure indicates that TM841 has the molecular function of fatty-acid binding and may play a role in the cellular functions of fatty acid transport or metabolism.

About this Structure

1MGP is a Single protein structure of sequence from Thermotoga maritima with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a hypothetical protein, TM841 of Thermotoga maritima, reveals its function as a fatty acid-binding protein., Schulze-Gahmen U, Pelaschier J, Yokota H, Kim R, Kim SH, Proteins. 2003 Mar 1;50(4):526-30. PMID:12577257

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